3QWP

Crystal structure of SET and MYND domain containing 3; Zinc finger MYND domain-containing protein 1

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000978	molecular_function	RNA polymerase II cis-regulatory region sequence-specific DNA binding
A	0000993	molecular_function	RNA polymerase II complex binding
A	0001162	molecular_function	RNA polymerase II intronic transcription regulatory region sequence-specific DNA binding
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005654	cellular_component	nucleoplasm
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006325	biological_process	chromatin organization
A	0006334	biological_process	nucleosome assembly
A	0008168	molecular_function	methyltransferase activity
A	0008270	molecular_function	zinc ion binding
A	0014904	biological_process	myotube cell development
A	0016740	molecular_function	transferase activity
A	0032259	biological_process	methylation
A	0042054	molecular_function	histone methyltransferase activity
A	0045184	biological_process	establishment of protein localization
A	0045944	biological_process	positive regulation of transcription by RNA polymerase II
A	0046872	molecular_function	metal ion binding
A	0071549	biological_process	cellular response to dexamethasone stimulus
A	0140939	molecular_function	histone H4 methyltransferase activity
A	0140954	molecular_function	histone H3K36 dimethyltransferase activity
A	0140999	molecular_function	histone H3K4 trimethyltransferase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 500

Chain	Residue
A	CYS62
A	CYS65
A	HIS83
A	CYS87

---

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 501

Chain	Residue
A	CYS49
A	CYS52
A	CYS71
A	CYS75

---

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 502

Chain	Residue
A	CYS261
A	CYS263
A	CYS266
A	CYS208

---

site_id	AC4
Number of Residues	22
Details	BINDING SITE FOR RESIDUE SAM A 510

Chain	Residue
A	ARG14
A	ASN16
A	TYR124
A	GLU130
A	ASN132
A	ASN181
A	SER202
A	LEU203
A	LEU204
A	ASN205
A	HIS206
A	TYR239
A	TYR257
A	PHE259
A	HOH491
A	HOH497
A	HOH512
A	HOH564
A	HOH567
A	HOH629
A	HOH679
A	GOL3001

---

site_id	AC5
Number of Residues	11
Details	BINDING SITE FOR RESIDUE GOL A 3001

Chain	Residue
A	ASN181
A	SER182
A	PHE183
A	SER202
A	ILE237
A	TYR239
A	TYR257
A	SAM510
A	HOH518
A	HOH751
A	GOL3004

---

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL A 3004

Chain	Residue
A	SER182
A	PHE183
A	THR184
A	HOH553
A	HOH591
A	GOL3001

---

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL A 3005

Chain	Residue
A	GLN191
A	LYS297
A	ASP332
A	ASP336
A	TYR358
A	GLN372
A	LYS375

---

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL A 3006

Chain	Residue
A	PHE151
A	GLN152
A	ILE159
A	GLN160
A	HOH724

---

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL A 3007

Chain	Residue
A	ARG140
A	ILE179
A	GLN256
A	HOH640

---

site_id	BC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL A 3008

Chain	Residue
A	ASP82
A	PHE110
A	ASP114
A	GLU142
A	HOH582
A	HOH685
A	HOH876

---

site_id	BC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL A 3009

Chain	Residue
A	CYS238
A	LEU240
A	MET242
A	HIS366
A	HOH494
A	HOH591
A	GOL3010

---

site_id	BC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL A 3010

Chain	Residue
A	ILE214
A	VAL215
A	HIS366
A	PRO367
A	VAL368
A	HOH520
A	HOH535
A	HOH553
A	GOL3009

---

Functional Information from PROSITE/UniProt

site_id	PS01360
Number of Residues	39
Details	ZF_MYND_1 Zinc finger MYND-type signature. Cdr..Cllgkeklmr........CsqCrvakYCsakCqkkawpd..Hkre.C

Chain	Residue	Details
A	CYS49-CYS87

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	236
Details	Domain: {"description":"SET","evidences":[{"source":"PROSITE-ProRule","id":"PRU00190","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	38
Details	Zinc finger: {"description":"MYND-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00134","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"APR-2010","submissionDatabase":"PDB data bank","title":"Crystal structure of human histone-lysine n-methyltransferase SMYD3 in complex with S-adenosyl-L-methionine.","authoringGroup":["Structural genomics consortium (SGC)"]}}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00134","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	5
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00190","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"APR-2010","submissionDatabase":"PDB data bank","title":"Crystal structure of human histone-lysine n-methyltransferase SMYD3 in complex with S-adenosyl-L-methionine.","authoringGroup":["Structural genomics consortium (SGC)"]}}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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